Menadione-induced oxidative stress accelerates onset of Emory mouse cataract in vivo

References

• Augusteyn, R. C. (1981) Protein modification in cataract: possible oxidative mechanisms. In Mechanisms of Cata-ract Formation in the Human Lens (Ed. Duncan, G.). Pp. 72-115. Academic Press, Inc., New York.
   Google Scholar
• Spector, A. (1984) Oxidation and cataract. In Ciba Foun-dation Symposium 106, Human Cataract Formation (Eds. Nugent, J. and Whelan, J.). Pp. 48–64. Pitman, London.
   Google Scholar
• Harding, J. J. (1991) Cataract Biochemistry, Epidemiology and Pharmacology. Chapman and Hall, London.
   Google Scholar
• Bhuyan, K. C., Bhuyan, D. K. and Podos, S. M. (1986) Lipid peroxidation in cataract of the human. Life Sciences, 38, 1463–1471.
   PubMed Web of Science ®Google Scholar
• Bhuyan, K. C. and Bhuyan, D. K. (1984) Molecular mech-anism of cataractogenesis: III. toxic metabolites of oxygen as initiators of lipid peroxidation and cataract. Curr. Eye Res. 3,67–81.
   Google Scholar
• Bhuyan, K. C. and Bhuyan, D. K. (1977) Regulation of hydrogen peroxide in eye humors: effect of 3-amino-1H- 1,2,4-triazole on catalase and glutathione peroxidase of rabbit eye. Biochim. Biophys. Acta, 497, 641–651.
   PubMed Web of Science ®Google Scholar
• Bhuyan, K. C. and Bhuyan, D. K. (1978) Superoxide dis-mutase of the eye: relative functions of superoxide dismu-tase and catalase in protecting the ocular lens from oxida-tive damage. Biochim. Biophys. Acta, 542, 28–38.
   Google Scholar
• Bhuyan, D. K. and Bhuyan, K. C. (1994) Assessment of oxidative stress to eye in animal model for cataract. In Oxygen Radicals in Biological Systems, Methods in Enzy-mology, Vol. 233 Part C (Ed. Packer, L.). Pp. 630–639. Academic Press, Inc., New York.
   Google Scholar
• Varma, S. D., Chand, D., Sharma, Y. R., Kuck, Jr., J. F. R. and Richards, R. D. (1984) Oxidative stress on lens and cataract formation: role of light and oxygen. Curr. Eye Res. 3, 35–57.
   Google Scholar
• Garner, W. H., Garner, M. H. and Spector, A. (1983) H202 induced uncoupling of bovine lens Na, K+-ATPase. Proc. Natl. Acad. Sci. USA, 80, 2044–2048.
   PubMed Web of Science ®Google Scholar
• Bhuyan, K. C., Bhuyan, D. K., Kuck, J. F. R., Jr., Kuck, K. D. and Kern, H. L. (1983) Increased lipid peroxidation and altered membrane functions in Emory mouse cataract. Curr. Eye Res. 2, 597–606.
   Google Scholar
• Giblin, F. J., McCready, J. P., Schrimscher, L. and Reddy, V. N. (1987) Peroxide-induced effects on lens cation trans-port following inhibition of glutathione reductase activity in vitro. Exp. Eye Res. 45, 77–91.
   PubMed Web of Science ®Google Scholar
• Zigler, J. S., Huang, Q.-L. and Du, X.-Y. (1989) Oxidative modification of lens crystallins by H202 and chelated iron. Free Radic. Biol. Med. 7, 499–505.
   Google Scholar
• Spector, A., Wang, G.-M., Wang, R.-R., Li, W.-C. and Kuszak, J. R. (1995) A brief photochemically induced oxi-dative insult causes irreversible lens damage and cataract. I. transparency and epithelial cell layer. Exp. Eye Res. 60, 471–481.
   Google Scholar
• Kuck, J. F. R., Kuwabara, T. and Kuck, K. D. (1981/1982) The Emory mouse cataract: an animal model for human senile cataract. Curr. Eye Res. 1, 643–649.
   Google Scholar
• Kuck, J. F. R. and Kuck, K. D. (1983) The Emory mouse cataract: loss of soluble protein, glutathione, protein sulf-hydryl and other changes. Exp. Eye Res. 36, 351–362.
   Google Scholar
• Thor, H., Smith, M. T., Hartzell, P., Bellomo, G., Jewell, S. A. and Orrenius, S. (1982) The metabolism of menadi-one (2-methyl-1,4-naphthoquinone) by isolated hepato-cytes. J. Biol. Chem. 257, 12419–12425.
   PubMed Web of Science ®Google Scholar
• Brunmark, A. and Cadenas, E. (1989) Redox and addition chemistry of quinoid compounds and its biological impli-cations. Free Radic. Biol. Med. 7, 435–477.
   PubMed Web of Science ®Google Scholar
• Rao, P. V, Krishna, C. M. and Zigler, J. S., Jr. (1992) Iden-tification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens: a novel NADPH: quinone oxidoreductase. J. Biol. Chem. 267, 96–102.
   Google Scholar
• Fridovich, I. (1978) The biology of oxygen radicals. Sci-ence, 201, 875–880.
   PubMed Web of Science ®Google Scholar
• Smith, M. T., Evans, C. G., Thor, H. and Orrenius, S. (1985) Quinone-induced oxidative injury to cells and tissues. In Oxidative Stress (Ed. Sies, H.). Pp. 91-113. Academic Press, Inc., London.
   Google Scholar
• van Heyningen, R. and Pine, A. (1967) The metabolism of naphthalene and its toxic effect on the eye. Biochem. I 102, 842–852.
   Google Scholar
• Xu, G.-T., Zigler, J. S., Jr. and Lou, M. F. (1992) Establish-ment of a naphthalene cataract model in vitro. Exp. Eye Res. 54, 73–81.
   PubMed Web of Science ®Google Scholar
• The Merck Index: An Encyclopedia of Chemicals and Drugs, 8th ed. (1968) (Ed. Stecher, P. G.). P. 652. Merck & Co., Inc., Rahway, NJ.
   Google Scholar
• Jones, K. M. (1969) Artificial substrates and biochemical reagents. In Data for Biochemical Research (Eds. Dawson, R. M. C., Elliott, D. C., Elliott, W. H. and Jones, K. M.). Pp. 438–439. Oxford University Press, New York.
   Google Scholar
• Ellman, G. L. (1958) A colorimetric method for determin-ing low concentrations of mercaptans. Arch. Biochem. Biophys. 74, 443–450.
   PubMed Web of Science ®Google Scholar
• Hildebrandt, A. G., Root, I., Tjoe, M. and Heinemeyer, G. (1978) Hydrogen peroxide in hepatic microsomes. In Methods in Enzymology, Vol. 52 (Eds. Fleischer, S. and Packer, L.). Pp. 342–350. Academic Press, Inc., New York.
   Google Scholar
• Fridovich, I. (1986) Cytochrome c. In CRC Handbook of Methods for Oxygen Radical Research (Ed. Greenwald, R. A.). Pp. 121–122. CRC Press, Inc., Boca Raton, FL.
   Google Scholar
• Halliwell, B. and Gutteridge, J. M. C. (1986) Hydroxyl radical assayed by aromatic hydroxylation and deoxyri-bose degradation. In CRC Handbook of Methods for Oxy-gen Radical Research (Ed. Greenwald, R. A.). Pp. 177–180. CRC Press, Inc., Boca Raton, FL.
   Google Scholar
• Dahle, L. K., Hill, E. G. and Holman, R. T. (1962) The thiobarbituric acid reaction and the autoxidation of poly-unsaturated fatty acid methyl esters. Arch. Biochem. Bio-phys. 98, 253–261.
   PubMed Web of Science ®Google Scholar
• Post, R. L. and Sen, A. K. (1967) Sodium and potassium-stimulated ATPase. In Methods in Enzymology, Vol. 10 (Eds. Estabrook, R. W. and Pullman, M. E.). Pp. 762–764. Academic Press, Inc., New York.
   Google Scholar
• Chen, P. S., Toribara, T. Y. and Warner, H. (1956) Microde-termination of phosphorus. Anal. Chem. 28, 1756–1758.
   Web of Science ®Google Scholar
• Hightower, K. R. and McCready, J. (1991) Effect of thiol reagents on Ca-ATPase in rabbit lens epithelium. Curr Eye Res. 10, 299–303.
   PubMed Web of Science ®Google Scholar
• Marklund, S. and Marklund, G. (1974) Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur I Biochem. 47, 469–474.
   PubMedGoogle Scholar
• Hochstein, P. and Utley, H. (1968) Hydrogen peroxide detoxification by glutathione peroxidase and catalase in rat liver homogenates. MoL PharmacoL 4, 574–579.
   PubMed Web of Science ®Google Scholar
• Goldstein, D. B. (1968) A method for assay of catalase with the oxygen cathode. Anal. Biochem. 24, 431–437.
   PubMed Web of Science ®Google Scholar
• Smith, P. F., Alberts, D. W. and Rush, G. F. (1987) Mena-dione-induced oxidative stress in hepatocytes isolated from fed and fasted rats: the role of NADPH-generating pathways. ToxicoL PharmacoL 89, 190–201.
   Google Scholar
• Reddan, J. R., Giblin, F. J., Dziedzic, D. C., McCready, J. P., Schrimscher, L. and Reddy, V. N. (1988) Influence of the activity of glutathione reductase on the response of cul- tured lens epithelial cells from young and old rabbits to hydrogen peroxide. Exp. Eye Res. 46, 209–221.
   PubMed Web of Science ®Google Scholar
• Janero, D. R. (1990) Malondialdehyde and thiobarbituric acid-reactivity as diagnostic indices of lipid peroxidation and peroxidative tissue injury. Free Radic. Biol. Med. 9, 515–540.
   PubMed Web of Science ®Google Scholar
• Scandalios, J. G. (1992) Molecular Biology of Free Radi-cal Scavenging Systems. Pp. 1–284. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
   Google Scholar